Structure analysis

Crystal structure of the first bromodomain (BD1) of human BRDT bound to NC-II-259

X-ray diffraction
1.98Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 11628.0 Å2
Buried surface area: 1468.71 Å2
Dissociation area: 734.36 Å2
Dissociation energy (ΔGdiss): 2.2 kcal/mol
Dissociation entropy (TΔSdiss): 11.48 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-176745

Macromolecules

Chains: A, B
Length: 113 amino acids
Theoretical weight: 13.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q58F21 (Residues: 29-137; Coverage: 12%)
Gene name: BRDT
Pfam: Bromodomain
InterPro:

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